Cathelicidins, multifunctional peptides of the innate immunity

Antimicrobial peptides of multicellular organisms

Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457 · see citing works

Endogenous Antimicrobial Peptides and Skin Infections in Atopic Dermatitis

Ong, P. Y., Ohtake, T., Brandt, C., Strickland, I., Boguniewicz, M., Ganz, T., Gallo, R. L., & Leung, D. Y. M. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa021481 · Cited by 1,960 · see citing works

Amphipathic, α-helical antimicrobial peptides

Tossi, A., Sandri, L., & Giangaspero, A. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)55:1 · Cited by 1,245 · see citing works

Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells

Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238 · see citing works

The role of cationic antimicrobial peptides in innate host defences

Hancock, R. E. W., & Diamond, G. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01823-0 · Cited by 1,233 · see citing works

Innate antimicrobial peptide protects the skin from invasive bacterial infection

Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198 · see citing works

Biology of the Syndecans: A Family of Transmembrane Heparan Sulfate Proteoglycans

Bernfield, M. R., Kokenyesi, R., Kato, M., Hinkes, M. T., Spring, J., Gallo, R. L., & Lose, E. J. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.002053 · Cited by 1,099 · see citing works

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., & Borregaard, N. (2001) · Blood · doi:10.1182/blood.v97.12.3951 · Cited by 894 · see citing works

An angiogenic role for the human peptide antibiotic LL-37/hCAP-18

Koczulla, R., von Degenfeld, G., Kupatt, C., Krötz, F., Stefan Zahler, A., GLOE, T. R., Issbrücker, K., Unterberger, P., Zaiou, M., Lebherz, C., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17545 · Cited by 864 · see citing works

The Expression of the Gene Coding for the Antibacterial Peptide LL-37 Is Induced in Human Keratinocytes during Inflammatory Disorders

Frohm, M., Agerberth, B., Ahangari, G., Ståhle‐Bäckdahl, M., Lidén, S., Wigzell, H., & Gudmundsson, G. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15258 · Cited by 803 · see citing works

Activities of LL-37, a Cathelin-Associated Antimicrobial Peptide of Human Neutrophils

Turner, J., Cho, Y., Dinh, N.-N., Waring, A. J., & Lehrer, R. I. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.9.2206 · Cited by 800 · see citing works

The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations

Agerberth, B., Charo, J., Werr, J., Olsson, B., Idali, F., Lindbom, L., Kiessling, R., Jörnvall, H., Wigzell, H., & Gudmundsson, G. H. (2000) · Blood · doi:10.1182/blood.v96.9.3086 · Cited by 758 · see citing works

The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface

Bals, R., Wang, X., ZASLOFF, M. A., & Wilson, J. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9541 · Cited by 745 · see citing works

Toward a phylogenetic classification of Primates based on DNA evidence complemented by fossil evidence.

Goodman, M., Porter, C. A., Czelusniak, J., Page, S. L., Schneider, H., Shoshani, J., Gunnell, G., & Groves, C. P. (1998) · Molecular Phylogenetics and Evolution · doi:10.1006/mpev.1998.0495 · Cited by 743 · see citing works

Antimicrobial peptides in mammalian and insect host defence

Lehrer, R. I., & Ganz, T. (1999) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)80005-3 · Cited by 723 · see citing works

The Human Antimicrobial Peptide LL-37 Is a Multifunctional Modulator of Innate Immune Responses

Scott, M. G., Davidson, D. J., Gold, M. R., Bowdish, D. M. E., & Hancock, R. E. W. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.7.3883 · Cited by 713 · see citing works

Cathelicidins: a novel protein family with a common proregion and a variable C‐terminal antimicrobial domain

Zanetti, M., Gennaro, R., & Romeo, D. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01050-o · Cited by 708 · see citing works

Mammalian defensins in immunity: more than just microbicidal

Yang, D., Biragyn, A., Kwak, L. W., & Oppenheim, J. J. (2002) · Trends in Immunology · doi:10.1016/s1471-4906(02)02246-9 · Cited by 696 · see citing works

Conformation-dependent Antibacterial Activity of the Naturally Occurring Human Peptide LL-37

Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., & Agerberth, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3718 · Cited by 662 · see citing works

Defensins of vertebrate animals

Lehrer, R. I., & Ganz, T. (2002) · Current Opinion in Immunology · doi:10.1016/s0952-7915(01)00303-x · Cited by 662 · see citing works

Formyl-peptide receptors revisited

Le, Y., MURPHY, P., & Wang, J. (2002) · Trends in Immunology · doi:10.1016/s1471-4906(02)02316-5 · Cited by 600 · see citing works

The Cathelicidin Anti-Microbial Peptide LL-37 is Involved in Re-Epithelialization of Human Skin Wounds and is Lacking in Chronic Ulcer Epithelium

Heilborn, J. D., Nilsson, M. F., Sørensen, O., Ståhle-Bäckdahl, M., Kratz, G., Weber, G., & Borregaard, N. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12069.x · Cited by 572 · see citing works

Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein

Larrick, J. W., Hirata, M., Balint, R. F., Lee, J. H., Zhong, J., & Wright, S. C. (1995) · Infection and Immunity · doi:10.1128/iai.63.4.1291-1297.1995 · Cited by 570 · see citing works

Cutaneous Injury Induces the Release of Cathelicidin Anti-Microbial Peptides Active Against Group A Streptococcus

Dorschner, R. A., Pestonjamasp, V. K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., Agerberth, B., Gudmundsson, G. H., & Gallo, R. L. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2001.01340.x · Cited by 567 · see citing works

FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis.

Agerberth, B., Gunne, H., Odeberg, J., Kogner, P., Boman, H. G., & Gudmundsson, G. H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.1.195 · Cited by 502 · see citing works

Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study

Pütsep, K., Carlsson, G., Boman, H. G., & Andersson, M. (2002) · The Lancet · doi:10.1016/s0140-6736(02)11201-3 · Cited by 499 · see citing works

Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL‐37

Schmidtchen, A., Frick, I.-M., Andersson, E., Tapper, H., & Björck, L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03146.x · Cited by 440 · see citing works

Physiologic Mechanisms of Postischemic Tissue Injury

Granger, D. N., & Korthuis, R. J. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.001523 · Cited by 436 · see citing works

Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator

Islam, D., Bandholtz, L., Nilsson, J., Wigzell, H., Christensson, B., Agerberth, B., & Gudmundsson, G. H. (2001) · Nature Medicine · doi:10.1038/84627 · Cited by 429 · see citing works

Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

Gallo, R. L., Kim, K. J., Bernfield, M. R., Kozak, C. A., Zanetti, M., Merluzzi, L., & Gennaro, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.20.13088 · Cited by 419 · see citing works

Cutting Edge: Mast Cell Antimicrobial Activity Is Mediated by Expression of Cathelicidin Antimicrobial Peptide

Nardo, A. D., Vitiello, A., & Gallo, R. L. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.5.2274 · Cited by 405 · see citing works

A cathelicidin family of human antibacterial peptide LL‐37 induces mast cell chemotaxis

Niyonsaba, F., Iwabuchi, K., Someya, A., Hirata, M., Matsuda, H., Ogawa, H., & Nagaoka, I. (2002) · Immunology · doi:10.1046/j.1365-2567.2002.01398.x · Cited by 401 · see citing works

PR39, a peptide regulator of angiogenesis

Li, J., Post, M. J., Volk, R., Gao, Y., Li, M., Métais, C., Sato, K., Tsai, J. C., Aird, W. C., ROSENBERG, R. D., et al. (2000) · Nature Medicine · doi:10.1038/71527 · Cited by 387 · see citing works

Bactericidal Activity of Mammalian Cathelicidin-Derived Peptides

Travis, S. M., Anderson, N. N., Forsyth, W. R., Espiritu, C., Conway, B. D., Greenberg, E. P., McCray, P. B., Lehrer, R. I., Welsh, M. J., & Tack, B. F. (2000) · Infection and Immunity · doi:10.1128/iai.68.5.2748-2755.2000 · Cited by 369 · see citing works

The Human Antibacterial Cathelicidin, hCAP-18, Is Synthesized in Myelocytes and Metamyelocytes and Localized to Specific Granules in Neutrophils

Sørensen, O. E., Arnljots, K., Cowland, J. B., Bainton, D. F., & Borregaard, N. (1997) · Blood · doi:10.1182/blood.v90.7.2796 · Cited by 364 · see citing works

Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds.

Gallo, R. L., Ono, M., Povsic, T. J., Page, C., Eriksson, E. K., Klagsbrun, M., & Bernfield, M. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11035 · Cited by 361 · see citing works

The Human Cationic Antimicrobial Protein (hCAP18), a Peptide Antibiotic, Is Widely Expressed in Human Squamous Epithelia and Colocalizes with Interleukin-6

Nilsson, M. F., Sandstedt, B., Sørensen, O. E., Weber, G., Borregaard, N., & Ståhle‐Bäckdahl, M. (1999) · Infection and Immunity · doi:10.1128/iai.67.5.2561-2566.1999 · Cited by 351 · see citing works

Amino acid sequence of PR‐39

Agerberth, B., Jong‐Youn, L. E. E., Bergman, T., Carlquist, M., Boman, H. G., Mutt, V., & Jörnvall, H. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16442.x · Cited by 348 · see citing works

hCAP‐18, a cathelin/pro‐bactenecin‐like protein of human neutrophil specific granules

Cowland, J. B., Johnsen, A. H., & Borregaard, N. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00634-l · Cited by 347 · see citing works

Rodent Phylogeny and a Timescale for the Evolution of Glires: Evidence from an Extensive Taxon Sampling Using Three Nuclear Genes

Huchon, D., Madsen, O., Sibbald, M. J. J. B., Ament, K., Stanhope, M. J., Catzeflis, F. M., JONG, W. W. D., & Douzery, E. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004164 · Cited by 336 · see citing works

Cathelicidins: a family of endogenous antimicrobial peptides

Lehrer, R. I., & Ganz, T. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200201000-00004 · Cited by 324 · see citing works

Augmentation of Innate Host Defense by Expression of a Cathelicidin Antimicrobial Peptide

Bals, R., Weiner, D. J., Moscioni, A. D., Meegalla, R. L., & Wilson, J. M. (1999) · Infection and Immunity · doi:10.1128/iai.67.11.6084-6089.1999 · Cited by 302 · see citing works

Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils

Gennaro, R., Skerlavaj, B., & Romeo, D. (1989) · Infection and Immunity · doi:10.1128/iai.57.10.3142-3146.1989 · Cited by 300 · see citing works

Cathelicidin Anti-Microbial Peptide Expression in Sweat, an Innate Defense System for the Skin

Murakami, M., Ohtake, T., Dorschner, R. A., Gallo, R. L., Schittek, B., & Garbe, C. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.19507.x · Cited by 290 · see citing works

Cationic Antimicrobial Peptides and Their Multifunctional Role in the Immune System

Scott, M. G., & Hancock, R. E. W. (2000) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v20.i5.40 · Cited by 283 · see citing works

Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37)

Yang, D., Chertov, O., & Oppenheim, J. J. (2001) · Journal of Leukocyte Biology · doi:10.1189/jlb.69.5.691 · Cited by 276 · see citing works

Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence

Zaiou, M., Nizet, V., & Gallo, R. L. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12132.x · Cited by 256 · see citing works

Biological Characterization of Two Novel Cathelicidin-derived Peptides and Identification of Structural Requirements for Their Antimicrobial and Cell Lytic Activities

Skerlavaj, B., Gennaro, R., Bagella, L., Merluzzi, L., Risso, A., & Zanetti, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28375 · Cited by 252 · see citing works

The role of mammalian antimicrobial peptides and proteins in awakening of innate host defenses and adaptive immunity

Yang, D., Chertov, O., & Oppenheim, J. J. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000914 · Cited by 236 · see citing works

Cathelicidins, essential gene-encoded mammalian antibiotics

Zaiou, M., & Gallo, R. L. (2002) · Journal of Molecular Medicine · doi:10.1007/s00109-002-0350-6 · Cited by 224 · see citing works

The Human Cationic Antimicrobial Protein (hCAP-18) Is Expressed in the Epithelium of Human Epididymis, Is Present in Seminal Plasma at High Concentrations, and Is Attached to Spermatozoa

Malm, J., Sørensen, O. E., Persson, T., Frohm‐Nilsson, M., Johansson, B., Bjartell, A. S., Lilja, H. G., Ståhle‐Bäckdahl, M., Borregaard, N., & Egesten, A. (2000) · Infection and Immunity · doi:10.1128/iai.68.7.4297-4302.2000 · Cited by 223 · see citing works

Gene‐Encoded Peptide Antibiotics and the Concept of Innate Immunity: An Update Review

Boman (1998) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.1998.00343.x · Cited by 222 · see citing works

Cathelicidin Antimicrobial Peptides are Expressed in Salivary Glands and Saliva

Murakami, M., Ohtake, T., Dorschner, R. A., & Gallo, R. L. (2002) · Journal of Dental Research · doi:10.1177/154405910208101210 · Cited by 215 · see citing works

Antimicrobial polypeptides in host defense of the respiratory tract

Ganz, T. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15218 · Cited by 213 · see citing works

Biochemical and Antibacterial Analysis of Human Wound and Blister Fluid

Frohm, M., Gunne, H., Bergman, A., Agerberth, B., Bergman, T., Boman, A., Lidén, S., Jörnvall, H., & Boman, H. G. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0086n.x · Cited by 212 · see citing works

An ELISA for hCAP-18, the cathelicidin present in human neutrophils and plasma

Sørensen, O. E., Cowland, J. B., Askaa, J., & Borregaard, N. (1997) · Journal of Immunological Methods · doi:10.1016/s0022-1759(97)00084-7 · Cited by 209 · see citing works

Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils.

Frank, R. W., Gennaro, R., Schneider, K., Przybylski, M., & Romeo, D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30595-1 · Cited by 199 · see citing works

Antimicrobial polypeptides in host defense of the respiratory tract

Ganz, T. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215218 · Cited by 191 · see citing works

Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model

Bals, R., Weiner, D. J., Meegalla, R. L., & Wilson, J. M. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6570 · Cited by 190 · see citing works

PR-39, a proline-rich antibacterial peptide that inhibits phagocyte NADPH oxidase activity by binding to Src homology 3 domains of p47 phox.

Shi, J. N., Ross, C. R., Leto, T. L., & Blecha, F. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.6014 · Cited by 185 · see citing works

Processing of Seminal Plasma hCAP-18 to ALL-38 by Gastricsin

Sørensen, O. E., Gram, L., Johnsen, A. H., Andersson, E., Bangsbøll, S., Tjabringa, G. S., Hiemstra, P. S., Malm, J., Egesten, A., & Borregaard, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301608200 · Cited by 166 · see citing works

Inhibition of ubiquitin-proteasome pathway–mediated IκBα degradation by a naturally occurring antibacterial peptide

Gao, Y., Lecker, S. H., Post, M. J., Hietaranta, A. J., Li, J., Volk, R., Li, M., Sato, K., Saluja, A. K., Steer, M. L., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9826 · Cited by 156 · see citing works

The role of mast cells in host defense and their subversion by bacterial pathogens

Féger, F., Varadaradjalou, S., Gao, Z., Abraham, S. N., & Arock, M. (2002) · Trends in Immunology · doi:10.1016/s1471-4906(01)02156-1 · Cited by 154 · see citing works

Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins

Scocchi, M., Skerlavaj, B., Romeo, D., & Gennaro, R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17324.x · Cited by 149 · see citing works

Primary structure of a new cysteine proteinase inhibitor from pig leucocytes

Ritonja, A., Kopitar, M., Jerala, R., & Türk, V. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81093-2 · Cited by 148 · see citing works

BMAP-28, an Antibiotic Peptide of Innate Immunity, Induces Cell Death through Opening of the Mitochondrial Permeability Transition Pore

Risso, A., Braidot, E., Sordano, M. C., Vianello, A., Macrı̀, F., Skerlavaj, B., Zanetti, M., Gennaro, R., & Bernardi, P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.6.1926-1935.2002 · Cited by 148 · see citing works

Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds

Cole, A. M., Shi, J., Ceccarelli, A., Kim, Y.-H., Park, A., & Ganz, T. (2001) · Blood · doi:10.1182/blood.v97.1.297 · Cited by 146 · see citing works

Cytotoxicity and Apoptosis Mediated by Two Peptides of Innate Immunity

Risso, A., Zanetti, M., & Gennaro, R. (1998) · Cellular Immunology · doi:10.1006/cimm.1998.1358 · Cited by 146 · see citing works

Bactenecins, defense polypeptides of bovine neutrophils, are generated from precursor molecules stored in the large granules.

Zanetti, M., Litteri, L., Gennaro, R., Horstmann, H., & Romeo, D. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.4.1363 · Cited by 146 · see citing works

Induction of oral tolerance to cellular immune responses in the absence of Peyer's patches

Spahn, T. W., Fontana, A., Faria, A. M. C., Slavin, A., Eugster, H., Zhang, X., Koni, P. A., Ruddle, N. H., Flavell, R. A., Rennert, P. D., et al. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200104)31:4 · Cited by 143 · see citing works

A novel granulocyte-derived peptide with lipopolysaccharide-neutralizing activity.

Larrick, J. W., Hirata, M., Zheng, H., Zhong, J., Bolin, D., Cavaillon, J., Warren, H. S., & Wright, S. C. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.1.231 · Cited by 142 · see citing works

Apolipoprotein A-I Binds and Inhibits the Human Antibacterial/Cytotoxic Peptide LL-37

Wang, Y., Agerberth, B., Löthgren, A., Almstedt, A., & Johansson, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33115 · Cited by 134 · see citing works

Chemoattractant properties of PR-39, a neutrophil antibacterial peptide

Huang, H.-J., Ross, C. R., & Blecha, F. (1997) · Journal of Leukocyte Biology · doi:10.1002/jlb.61.5.624 · Cited by 133 · see citing works

Structure and Biology of Cathelicidins

Zanetti, M., Gennaro, R., Scocchi, M., & Skerlavaj, B. (2002) · Advances in experimental medicine and biology · doi:10.1007/0-306-46831-x_17 · Cited by 132 · see citing works

The cDNA of the neutrophil antibiotic Bac5 predicts a pro-sequence homologous to a cysteine proteinase inhibitor that is common to other neutrophil antibiotics.

Zanetti, M., Sal, G. D., Storici, P., Schneider, C., & Romeo, D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54182-x · Cited by 128 · see citing works

Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39.

Gudmundsson, G. H., Magnússon, K. P., Chowdhary, B. P., Johansson, M., Andersson, L., & Boman, H. G. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.15.7085 · Cited by 125 · see citing works

Complementary DNA sequence of rabbit CAP18—A unique lipopolysaccharide binding protein

Larrick, J. W., Morgan, J. G., Palings, I., Hirata, M., & Yen, M. H. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91350-l · Cited by 125 · see citing works

Localization and genomic organization of sheep antimicrobial peptide genes

Huttner, K. M., Lambeth, M. R., Burkin, H. R., Burkin, D. J., & Broad, T. E. (1998) · Gene · doi:10.1016/s0378-1119(97)00569-6 · Cited by 118 · see citing works

The Human Antibacterial Cathelicidin, hCAP-18, Is Bound to Lipoproteins in Plasma

Sørensen, O. E., Bratt, T., Johnsen, A. H., Madsen, M. T., & Borregaard, N. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22445 · Cited by 118 · see citing works

Purification and Properties of Proline-Rich Antimicrobial Peptides from Sheep and Goat Leukocytes

Валерьевна, Ш. О., Brogden, K. A., Zhao, C., Nguyen, T. X., Kokryakov, V. N., & Lehrer, R. I. (1999) · Infection and Immunity · doi:10.1128/iai.67.8.4106-4111.1999 · Cited by 118 · see citing works

PR-39, a Syndecan-inducing Antimicrobial Peptide, Binds and Affects p130Cas

Chan, Y. R., & Gallo, R. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.28978 · Cited by 115 · see citing works

Protective Effects of a Human 18-Kilodalton Cationic Antimicrobial Protein (CAP18)-Derived Peptide against Murine Endotoxemia

Kirikae, T., Hirata, M., Yamasu, H., Kirikae, F., Tamura, H., Kayama, F., Nakatsuka, K., Yokochi, T., & Nakano, M. (1998) · Infection and Immunity · doi:10.1128/iai.66.5.1861-1868.1998 · Cited by 112 · see citing works

Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA

Storici, P., Scocchi, M., Tossi, A., Gennaro, R., & Zanetti, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80214-9 · Cited by 109 · see citing works

SMAP‐29 has two LPS‐binding sites and a central hinge

Tack, B. F., Sawai, M. V., Kearney, W. R., Robertson, A. D., Sherman, M. A., Wang, W., Hong, T., Boo, L. M., Wu, H., Waring, A. J., et al. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2002.02751.x · Cited by 107 · see citing works

A novel type of cytoplasmic granule in bovine neutrophils.

Gennaro, R., Dewald, B., Horisberger, U., Gubler, H. U., & Baggiolini, M. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.96.6.1651 · Cited by 106 · see citing works

Cathelicidin peptides as candidates for a novel class of antimicrobials

Zanetti, M., Gennaro, R., Skerlavaj, B., Tomasinsig, L., & Circo, R. (2002) · Current Pharmaceutical Design · doi:10.2174/1381612023395457 · Cited by 105 · see citing works

cDNA sequences of three sheep myeloid cathelicidins

Bagella, L., Scocchi, M., & Zanetti, M. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01285-3 · Cited by 103 · see citing works

PMAP-37, a Novel Antibacterial Peptide from Pig Myeloid Cells. cDNA Cloning, Chemical Synthesis and Activity

Tossi, A., Scocchi, M., Zanetti, M., Storici, P., & Gennaro, R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20344.x · Cited by 100 · see citing works

Identification of a new member of the protegrin family by cDNA cloning

Zhao, C., Liu, L., & Lehrer, R. I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00493-5 · Cited by 100 · see citing works

Structural organization of the bovine cathelicidin gene family and identification of a novel member1

Scocchi, M., Wang, S., & Zanetti, M. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01310-0 · Cited by 94 · see citing works

Stimulus-induced maturation of probactenecins, precursors of neutrophil antimicrobial polypeptides

Zanetti, M., Litteri, L., Griffiths, G. W., Gennaro, R., & Romeo, D. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.146.12.4295 · Cited by 93 · see citing works

Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells.

Zanetti, M., Storici, P., Tossi, A., Scocchi, M., & Gennaro, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37128-4 · Cited by 92 · see citing works

Physiologic Mechanisms of Post-Ischemic Tissue Injury

Granger, D. N. (1995) · Annual Review of Physiology · doi:10.1146/annurev.physiol.57.1.311 · Cited by 92 · see citing works

Characterization of a rabbit cationic protein (CAP18) with lipopolysaccharide-inhibitory activity

Hirata, M., Shimomura, Y., Yoshida, M., Morgan, J. G., Palings, I., Wilson, D., Yen, M. H., Wright, S. C., & Larrick, J. W. (1994) · Infection and Immunity · doi:10.1128/iai.62.4.1421-1426.1994 · Cited by 88 · see citing works

The structure of porcine protegrin genes

Zhao, C., Ganz, T., & Lehrer, R. I. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00633-k · Cited by 85 · see citing works

Antibacterial 15-kDa protein isoforms (p15s) are members of a novel family of leukocyte proteins.

Levy, O., Weiss, J. P., Zarember, K. A., Ooi, C. E., & Elsbach, P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53425-6 · Cited by 83 · see citing works

Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide

Mahoney, M. M., Lee, A. Y., Brezinski-Caliguri, D. J., & Huttner, K. M. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01390-3 · Cited by 82 · see citing works

A cDNA Derived from Pig Bone Marrow Cells Predicts a Sequence Identical to the Intestinal Antibacterial Peptide PR-39

Storici, P., & Zanetti, M. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2358 · Cited by 82 · see citing works

Structures of genes for two cathelin‐associated antimicrobial peptides: prophenin‐2 and PR‐39

Zhao, C., Ganz, T., & Lehrer, R. I. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01237-3 · Cited by 78 · see citing works

Isolation of human cationic antimicrobial protein-18 from seminal plasma and its association with prostasomes

Andersson, E. (2002) · Human Reproduction · doi:10.1093/humrep/17.10.2529 · Cited by 73 · see citing works

Novel cathelicidins in horse leukocytes

Scocchi, M., Bontempo, D., Boscolo, S., Tomasinsig, L., Giulotto, E., & Zanetti, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01097-2 · Cited by 70 · see citing works

Purification and Structural Characterization of Bovine Cathelicidins, Precursors of Antimicrobial Peptides

Storici, P., Tossi, A., Lenar≷cic̆, B., & Romeo, D. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0769w.x · Cited by 70 · see citing works

CDNA cloning of the neutrophil bactericidal peptide indolicidin

Sal, G. D., Storici, P., Schneider, C., Romeo, D., & Zanetti, M. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81517-7 · Cited by 68 · see citing works

Chemotactic and protease‐inhibiting activities of antibiotic peptide precursors

Verbanac, D., Zanetti, M., & Romeo, D. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81287-a · Cited by 67 · see citing works

Interaction of two proline-rich sequences of cell adhesion kinase β with SH3 domains of p130Cas-related proteins and a GTPase-activating protein, Graf

Ohba, T., Ishino, M., Aoto, H., & Sasaki, T. (1998) · Biochemical Journal · doi:10.1042/bj3301249 · Cited by 65 · see citing works

A Novel cDNA Sequence Encoding a Pig Leukocyte Antimicrobial Peptide with a Cathelin-like Pro-sequence

Storici, P., & Zanetti, M. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2403 · Cited by 64 · see citing works

cDNA sequence analysis of an antibiotic dodecapeptide from neutrophils

Storici, P., Sal, G. D., Schneider, C., & Zanetti, M. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80971-i · Cited by 64 · see citing works

RL-37, an Alpha-Helical Antimicrobial Peptide of the Rhesus Monkey

Zhao, C., Nguyen, T. X., Boo, L. M., Hong, T., Espiritu, C., Orlov, D. S., Wang, W., Waring, A. J., & Lehrer, R. I. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.10.2695-2702.2001 · Cited by 62 · see citing works

Phylogeny, processing and expression of the rat Cathelicidin rCRAMP: a model for innate antimicrobial peptides

Term�n, S., Tollin, M., Olsson, B., Svenberg, T., Agerberth, B., & Gudmundsson, G. H. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s000180300045 · Cited by 57 · see citing works

Isolation of cDNA Encoding Guinea Pig Neutrophil Cationic Antibacterial Polypeptide of 11 kDa (CAP11) and Evaluation of CAP11 mRNA Expression during Neutrophil Maturation

Nagaoka, I., Tsutsumi‐Ishii, Y., Yomogida, S., & Yamashita, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22742 · Cited by 57 · see citing works

Structure of the Cathelicidin Motif of Protegrin-3 Precursor

Sanchez, J.-F., Hoh, F., Strub, M., Aumelas, A., & Dumas, C. (2002) · Structure · doi:10.1016/s0969-2126(02)00859-6 · Cited by 54 · see citing works

Interaction of hagfish cathelicidin antimicrobial peptides with model lipid membranes

Basáñez, G., Shinnar, A. E., & Zimmerberg, J. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03651-7 · Cited by 54 · see citing works

Rhesus Monkey ( Macaca mulatta ) Mucosal Antimicrobial Peptides Are Close Homologues of Human Molecules

Bals, R., Lang, C., Weiner, D. J., Vogelmeier, C. F., WELSCH, U. N., & Wilson, J. M. (2001) · Clinical and Diagnostic Laboratory Immunology · doi:10.1128/cdli.8.2.370-375.2001 · Cited by 54 · see citing works

PR-39, a proline/arginine-rich antimicrobial peptide, prevents postischemic microvascular dysfunction

Korthuis, R. J., Gute, D. C., Blecha, F., & Ross, C. R. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.3.h1007 · Cited by 48 · see citing works

Molecular cloning of Bac7, a proline‐ and arginine‐rich antimicrobial peptide from bovine neutrophils

Scocchi, M., Romeo, D., & Zanetti, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00954-6 · Cited by 48 · see citing works

PI3‐kinase p85α Is a Target Molecule of Proline‐rich Antimicrobial Peptide to Suppress Proliferation of ras‐Transformed Cells

Tanaka, K., Fujimoto, Y., Suzuki, M., Suzuki, Y., Ohtake, T., Saito, H., & Kohgo, Y. (2001) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.2001.tb01187.x · Cited by 45 · see citing works

Inducible expression of an antimicrobial peptide of the innate immunity in polymorphonuclear leukocytes

Tomasinsig, L., Scocchi, M., Loreto, C. D., Artico, D., & Zanetti, M. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.72.5.1003 · Cited by 37 · see citing works

A novel murine cathelin‐like protein expressed in bone marrow

Popsueva, A. E., Zinovjeva, M. V., Visser, J. W. M., Zijlmans, J. M. J. M., Fibbe, W. E., & Belyavsky, A. V. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00692-8 · Cited by 36 · see citing works

Molecular cloning of a novel myeloid granule protein

Moscinski, L. C., & Hill, B. (1995) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240590404 · Cited by 32 · see citing works

Cloning and sequencing of SOB3, a human gene coding for a sperm protein homologous to an antimicrobial protein and potentially involved in zona pellucida binding

Hammami‐Hamza, S., Doussau, M., Bernard, J., Rogier, E., Duquenne, C., Richard, Y., Lefèvre, A., & Finaz, C. (2001) · Molecular Human Reproduction · doi:10.1093/molehr/7.7.625 · Cited by 29 · see citing works

Short Communication

Štrukelj, B., Pungerčar, J., Kopitar, G., Renko, M., Lenar≷cic̆, B., Berbić, S., & Türk, V. (1995) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1995.376.8.507 · Cited by 20 · see citing works

Six antimicrobial peptide genes of the cathelicidin family map to bovine chromosome 22q24 by fluorescence in situ hybridization

Castiglioni, B., Scocchi, M., Zanetti, M., & Ferretti, L. (2008) · Cytogenetics and Cell Genetics · doi:10.1159/000134492 · Cited by 17 · see citing works

Conservation Within Artiodactyls of an AATA Interrupt in the IGF-I Microsatellite for 19–35 Million Years

Shariflou, M. R., & Moran, C. (2000) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a026345 · Cited by 16 · see citing works

Wielding more power over angiogenesis

Habeck, M. (2000) · Molecular Medicine Today · doi:10.1016/s1357-4310(00)01690-7 · Cited by 2 · see citing works

Peptide Antimicrobial Agents

Jenssen, H., Hamill, P., & Hancock, R. E. W. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.00056-05 · Cited by 2,532 · see citing works

Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide

Lande, R., Gregorio, J., Facchinetti, V., Chatterjee, B., Wang, Y.-H., Homey, B., Cao, W., Wang, Y.-H., Su, B., Nestle, F. O., et al. (2007) · Nature · doi:10.1038/nature06116 · Cited by 1,910 · see citing works

How dying cells alert the immune system to danger

Kono, H., & Rock, K. L. (2008) · Nature Reviews Immunology · doi:10.1038/nri2215 · Cited by 1,737 · see citing works

The expanding scope of antimicrobial peptide structures and their modes of action

Nguyen, L. T., Haney, E. F., & Vogel, H. J. (2011) · Trends in biotechnology · doi:10.1016/j.tibtech.2011.05.001 · Cited by 1,608 · see citing works

Antimicrobial host defence peptides: functions and clinical potential

Mookherjee, N., Anderson, M. A., Haagsman, H. P., & Davidson, D. J. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0058-8 · Cited by 1,502 · see citing works

Neutrophils Activate Plasmacytoid Dendritic Cells by Releasing Self-DNA–Peptide Complexes in Systemic Lupus Erythematosus

Lande, R., Ganguly, D., Facchinetti, V., Frasca, L., Conrad, C., Gregorio, J. D., Meller, S., Chamilos, G., Sebasigari, R., Riccieri, V., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3001180 · Cited by 1,306 · see citing works

AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense

Lai, Y., & Gallo, R. L. (2009) · Trends in Immunology · doi:10.1016/j.it.2008.12.003 · Cited by 1,275 · see citing works

Immune evasion by staphylococci

Foster, T. J. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1289 · Cited by 1,214 · see citing works

Mammalian defensins in the antimicrobial immune response

Selsted, M. E., & Ouellette, A. J. (2005) · Nature Immunology · doi:10.1038/ni1206 · Cited by 1,196 · see citing works

LL-37, the only human member of the cathelicidin family of antimicrobial peptides

Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.030 · Cited by 1,049 · see citing works

The antimicrobial peptides and their potential clinical applications.

Lei, J., Sun, L., Huang, S., Zhu, C., Li, P., He, J., Mackey, V., Coy, D. H., & He, Q. (2019) · PubMed Central · Cited by 1,043 · see citing works

The Alzheimer's Disease-Associated Amyloid β-Protein Is an Antimicrobial Peptide

Soscia, S. J., Kirby, J. E., Washicosky, K. J., Tucker, S. M., Ingelsson, M., Hyman, B., Burton, M. A., Goldstein, L. E., Duong, S., Tanzi, R. E., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009505 · Cited by 1,060 · see citing works

The Inflammatory Response to Cell Death

Rock, K. L., & Kono, H. (2007) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.3.121806.151456 · Cited by 945 · see citing works

Increased serine protease activity and cathelicidin promotes skin inflammation in rosacea

Yamasaki, K., Nardo, A. D., Bardan, A., Murakami, M., Ohtake, T., Coda, A. B., Dorschner, R. A., Bonnart, C., Descargues, P., Hovnanian, A., et al. (2007) · Nature Medicine · doi:10.1038/nm1616 · Cited by 852 · see citing works

Antimicrobial peptides: key components of the innate immune system

Pasupuleti, M., Schmidtchen, A., & Malmsten, M. (2011) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2011.594423 · Cited by 804 · see citing works

Alarmins: chemotactic activators of immune responses

Oppenheim, J. J., & Yang, D. (2005) · Current Opinion in Immunology · doi:10.1016/j.coi.2005.06.002 · Cited by 780 · see citing works

Genome analysis of the platypus reveals unique signatures of evolution

paper, A. L. O. A. A. T. A. A. A. T. E. O. T. (2008) · Nature · doi:10.1038/nature06936 · Cited by 719 · see citing works

Role of intestinal microbiota and metabolites on gut homeostasis and human diseases

Lin, L., & Zhang, J. (2017) · BMC Immunology · doi:10.1186/s12865-016-0187-3 · Cited by 731 · see citing works

Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus

Mygind, P. H., Fischer, R. L., Schnorr, K. M., Hansen, M. T., Sönksen, C. P., Ludvigsen, S., Raventós, D., Buskov, S., Christensen, B. B., Maria, L. D., et al. (2005) · Nature · doi:10.1038/nature04051 · Cited by 655 · see citing works

Cathelicidins: family of antimicrobial peptides. A review

Kościuczuk, E. M., Lisowski, P., Jarczak, J., Strzałkowska, N., Jóźwik, A., Horbańczuk, J. O., Krzyżewski, J., Zwierzchowski, L., & Bagnicka, E. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-1997-x · Cited by 571 · see citing works

Modulation of the TLR-Mediated Inflammatory Response by the Endogenous Human Host Defense Peptide LL-37

Mookherjee, N., Brown, K. L., Bowdish, D. M. E., Doria, S., Falsafi, R., Hokamp, K., Roche, F. M., Mu, R., Doho, G., Pistolic, J., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.4.2455 · Cited by 562 · see citing works

The Front Line of Enteric Host Defense against Unwelcome Intrusion of Harmful Microorganisms: Mucins, Antimicrobial Peptides, and Microbiota

Liévin-Le Moal, V., & Servin, A. L. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.19.2.315-337.2006 · Cited by 568 · see citing works

Human Antimicrobial Peptides: Defensins, Cathelicidins and Histatins

Smet, K. D., & Contreras, R. (2005) · Biotechnology Letters · doi:10.1007/s10529-005-0936-5 · Cited by 561 · see citing works

Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus -Derived Proteinases

Sieprawska‐Lupa, M., Mydel, P. M., Krawczyk, K., Wójcik, K., Puklo, M., Lupa, B., Suder, P., Silberring, J., Reed, M. S., Pohl, J., et al. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.12.4673-4679.2004 · Cited by 552 · see citing works

The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection

Chromek, M., Slamová, Z., Bergman, P., Kovács, L., Podracká, L., Ehrén, I., Hökfelt, T., Gudmundsson, G. H., Gallo, R. L., Agerberth, B., et al. (2006) · Nature Medicine · doi:10.1038/nm1407 · Cited by 652 · see citing works

Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance

Guilhelmelli, F., Vilela, N., Albuquerque, P., Derengowski, L. D. S., Silva-Pereira, I., & Kyaw, C. M. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00353 · Cited by 548 · see citing works

The antimicrobial peptide LL37 is a T-cell autoantigen in psoriasis

Lande, R., Botti, E., Jandus, C., Dojcinovic, D., Fanelli, G., Conrad, C., Chamilos, G., Feldmeyer, L., Marinari, B., Chon, S. Y., et al. (2014) · Nature Communications · doi:10.1038/ncomms6621 · Cited by 541 · see citing works

Human Antimicrobial Peptides and Proteins

Wang, G. (2014) · Pharmaceuticals · doi:10.3390/ph7050545 · Cited by 528 · see citing works

Defensins in innate antiviral immunity

Klotman, M. E., & Chang, T. L. (2006) · Nature Reviews Immunology · doi:10.1038/nri1860 · Cited by 471 · see citing works

Interactions between Bacteria and Bile Salts in the Gastrointestinal and Hepatobiliary Tracts

Urdaneta, V., & Casadesús, J. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00163 · Cited by 449 · see citing works

Kallikrein‐mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin

Yamasaki, K., Schauber, J., Coda, A. B., Lin, H. C., Dorschner, R. A., Schechter, N. M., Bonnart, C., Descargues, P., Hovnanian, A., & Gallo, R. L. (2006) · The FASEB Journal · doi:10.1096/fj.06-6075com · Cited by 463 · see citing works

Primate defensins

Lehrer, R. I. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro976 · Cited by 455 · see citing works

The nervous system and innate immunity: the neuropeptide connection

Brogden, K. A., Guthmiller, J. M., Salzet, M., & ZASLOFF, M. A. (2005) · Nature Immunology · doi:10.1038/ni1209 · Cited by 445 · see citing works

The role of astrocytes in amyloid production and Alzheimer's disease

Frost, G. R., & Li, Y. (2017) · Open Biology · doi:10.1098/rsob.170228 · Cited by 435 · see citing works

Innate immunity in aging: impact on macrophage function

Plowden, J., Renshaw‐Hoelscher, M., Engleman, C., Katz, J. M., & Sambhara, S. R. (2004) · Aging Cell · doi:10.1111/j.1474-9728.2004.00102.x · Cited by 430 · see citing works

Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment

Mader, J. S., & Hoskin, D. W. (2006) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.15.8.933 · Cited by 425 · see citing works

Vitamin D and immune function: an overview

Hewison, M. (2011) · Proceedings of The Nutrition Society · doi:10.1017/s0029665111001650 · Cited by 424 · see citing works

Multi-organ proteomic landscape of COVID-19 autopsies

Nie, X., Qian, L.-J., Sun, R., Huang, B., Dong, X., Xiao, Q., Zhang, Q.-S., Lu, T., Yue, L., Chen, S., et al. (2020) · medRxiv · doi:10.1016/j.cell.2021.01.004 · Cited by 373 · see citing works

Antimicrobial Peptides: Old Molecules with New Ideas

Nakatsuji, T., & Gallo, R. L. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.387 · Cited by 397 · see citing works

Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications

Deslouches, B., & Di, Y. P. (2017) · Oncotarget · doi:10.18632/oncotarget.16743 · Cited by 391 · see citing works

Vitamin D Signaling, Infectious Diseases, and Regulation of Innate Immunity

White, J. H. (2008) · Infection and Immunity · doi:10.1128/iai.00353-08 · Cited by 381 · see citing works

Antiviral Activity and Increased Host Defense against Influenza Infection Elicited by the Human Cathelicidin LL-37

Barlow, P. G., Svoboda, P., Mackellar, A., Nash, A. A., York, I. A., Pohl, J., Davidson, D. J., & Donis, R. O. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025333 · Cited by 357 · see citing works

Membrane targeting cationic antimicrobial peptides

Ciumac, D., Gong, H., Hu, X., & Lu, J. R. (2018) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2018.10.103 · Cited by 353 · see citing works

Association of low serum 25-hydroxyvitamin D levels and mortality in the critically ill*

Braun, A. B., Chang, D., Mahadevappa, K., Gibbons, F. K., Liu, Y., Giovannucci, E. L., & Christopher, K. B. (2011) · Critical Care Medicine · doi:10.1097/ccm.0b013e318206ccdf · Cited by 352 · see citing works

Oral Microbiome: A Review of Its Impact on Oral and Systemic Health

Krishnamurthy, H. K., Bosco, J., Jayaraman, V., Krishna, K., Wang, T., Bei, K., & Rajasekaran, J. J. (2024) · Microorganisms · doi:10.3390/microorganisms12091797 · Cited by 402 · see citing works

Antibiotics, Resistome and Resistance Mechanisms: A Bacterial Perspective

Sultan, I., Rahman, S., Jan, A. T., Siddiqui, M. T., Mondal, A. H., & Haq, Q. M. R. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02066 · Cited by 326 · see citing works

When two is better than one: macrophages and neutrophils work in concert in innate immunity as complementary and cooperative partners of a myeloid phagocyte system

Silva, M. T. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0809549 · Cited by 321 · see citing works

Improved outcome in shigellosis associated with butyrate induction of an endogenous peptide antibiotic

Raqib, R., Sarker, P., Bergman, P., Ara, G., Lindh, M., Sack, D. A., Islam, K., Gudmundsson, G. H., Andersson, J., & Agerberth, B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602888103 · Cited by 317 · see citing works

Immunomodulatory Activities of Small Host Defense Peptides

Bowdish, D. M. E., Davidson, D. J., Scott, M. G., & Hancock, R. E. W. (2005) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.49.5.1727-1732.2005 · Cited by 317 · see citing works

Antimicrobial Activity of Mesenchymal Stem Cells: Current Status and New Perspectives of Antimicrobial Peptide-Based Therapies

Alcayaga‐Miranda, F., Cuenca, J., & Khoury, M. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00339 · Cited by 297 · see citing works

Antimicrobial Peptides: Versatile Biological Properties

Muthuirulan, P., Gunasekaran, P., & Rajendhran, J. (2013) · International Journal of Peptides · doi:10.1155/2013/675391 · Cited by 298 · see citing works

The roles of cathelicidin LL-37 in immune defences and novel clinical applications

Nijnik, A., & Hancock, R. E. W. (2008) · Current Opinion in Hematology · doi:10.1097/moh.0b013e32831ac517 · Cited by 287 · see citing works

Solution Structures of Human LL-37 Fragments and NMR-Based Identification of a Minimal Membrane-Targeting Antimicrobial and Anticancer Region

Li, X., Li, Y., Han, H., Miller, D. W., & Wang, G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0584875 · Cited by 285 · see citing works

Butyrate Enhances Disease Resistance of Chickens by Inducing Antimicrobial Host Defense Peptide Gene Expression

Sunkara, L. T., Achanta, M., Schreiber, N. B., Bommineni, Y. R., Dai, G., Jiang, W., Lamont, S. J., Lillehoj, H. S., Beker, A., Teeter, R. G., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027225 · Cited by 279 · see citing works

Structure-Function Relationships among Human Cathelicidin Peptides: Dissociation of Antimicrobial Properties from Host Immunostimulatory Activities

Braff, M. H., Hawkins, M. A., Nardo, A. D., López‐García, B., Howell, M. D., Wong, C., Lin, K. H., Streib, J. E., Dorschner, R. A., Leung, D. Y. M., et al. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.7.4271 · Cited by 275 · see citing works

Sterile inflammation and pregnancy complications: a review

Nadeau‐Vallée, M., Obari, D., Palacios, J. L., Brien, M., Duval, C., Chemtob, S., & Girard, S. (2016) · Reproduction · doi:10.1530/rep-16-0453 · Cited by 274 · see citing works

Defensins in innate immunity

Hazlett, L. D., & Wu, M. (2010) · Cell and Tissue Research · doi:10.1007/s00441-010-1022-4 · Cited by 268 · see citing works

Immunomodulatory Properties of Defensins and Cathelicidins

Bowdish, D. M. E., Davidson, D. J., & Hancock, R. E. W. (2006) · Current topics in microbiology and immunology · doi:10.1007/3-540-29916-5_2 · Cited by 268 · see citing works

The porcine innate immune system: an update

Mair, K. H., Sedlak, C., Käser, T., Pasternak, A., Levast, B., Gerner, W., Saalmüller, A., Summerfield, A., Gerdts, V., Wilson, H. L., et al. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.03.022 · Cited by 264 · see citing works

The role of microorganisms in atopic dermatitis

Baker, B. S. (2006) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2005.02980.x · Cited by 262 · see citing works

Staphylococcus colonization of the skin and antimicrobial peptides

Otto, M. J. (2010) · Expert Review of Dermatology · doi:10.1586/edm.10.6 · Cited by 261 · see citing works

Vitamin D metabolism and signaling in the immune system

White, J. H. (2011) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-011-9195-z · Cited by 261 · see citing works

Innate Immune Cells in Liver Inflammation

Liaskou, E., Wilson, D. V., & Oo, Y. H. (2012) · Mediators of Inflammation · doi:10.1155/2012/949157 · Cited by 255 · see citing works

The immunology of sepsis

Sriskandan, S., & Altmann, D. M. (2007) · The Journal of Pathology · doi:10.1002/path.2274 · Cited by 254 · see citing works

The role of the purinergic P2X7 receptor in inflammation

Lister, M. F., Sharkey, J., Sawatzky, D. A., Hodgkiss, J. P., Davidson, D. J., Rossi, A. G., & Finlayson, K. (2007) · Journal of Inflammation · doi:10.1186/1476-9255-4-5 · Cited by 255 · see citing works

Vitamin D Induces the Antimicrobial Protein hCAP18 in Human Skin

Weber, G., Heilborn, J. D., Chamorro, C. I., Hammarsjö, A., Törmä, H., & Ståhle, M. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23687.x · Cited by 251 · see citing works

Human Cathelicidin (LL-37), a Multifunctional Peptide, is Expressed by Ocular Surface Epithelia and has Potent Antibacterial and Antiviral Activity

Gordon, Y. J., Huang, L. C. L., Romanowski, E. G., Yates, K. A., Proske, R. J., & McDermott, A. M. (2005) · Current Eye Research · doi:10.1080/02713680590934111 · Cited by 251 · see citing works

Antimicrobial peptides, conventional antibiotics, and their synergistic utility for the treatment of drug‐resistant infections

Zhu, Y., Hao, W., Wang, X., Ouyang, J., Deng, X., Yu, H., & Wang, Y. (2022) · Medicinal Research Reviews · doi:10.1002/med.21879 · Cited by 254 · see citing works

Host defense peptides and their antimicrobial-immunomodulatory duality

Steinstraesser, L., Kraneburg, U. M., Jacobsen, F., & Al‐Benna, S. (2010) · Immunobiology · doi:10.1016/j.imbio.2010.07.003 · Cited by 245 · see citing works

Human Cathelicidin LL-37 Is a Chemoattractant for Eosinophils and Neutrophils That Acts via Formyl-Peptide Receptors

Tjabringa, G. S., Ninaber, D. K., Drijfhout, J. W., Rabe, K. F., & Hiemstra, P. S. (2006) · International Archives of Allergy and Immunology · doi:10.1159/000092305 · Cited by 246 · see citing works

Snake Cathelicidin from Bungarus fasciatus Is a Potent Peptide Antibiotics

Wang, Y., Hong, J., Liu, X., Yang, H., Liu, R., Wu, J., Wang, A., Lin, D., & Lai, R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003217 · Cited by 243 · see citing works

Identification and Functional Characterization of Three Chicken Cathelicidins with Potent Antimicrobial Activity

Xiao, Y., Cai, Y., Bommineni, Y. R., Fernando, S. C., Prakash, O., Gilliland, S. E., & Zhang, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507180200 · Cited by 240 · see citing works

Mas-related Gene X2 (MrgX2) Is a Novel G Protein-coupled Receptor for the Antimicrobial Peptide LL-37 in Human Mast Cells

Subramanian, H., Gupta, K., Guo, Q., Price, R. L., & Ali, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277152 · Cited by 239 · see citing works

Cathelicidin Mediates Innate Intestinal Defense against Colonization with Epithelial Adherent Bacterial Pathogens

Iimura, M., Gallo, R. L., Hase, K., Miyamoto, Y., Eckmann, L., & Kagnoff, M. F. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.8.4901 · Cited by 236 · see citing works

Vitamin D: sources, physiological role, biokinetics, deficiency, therapeutic use, toxicity, and overview of analytical methods for detection of vitamin D and its metabolites

Janoušek, J., Pilařová, V., Macáková, K., Nomura, A., Veiga-Matos, J., da Silva, D. D., Remião, F., Saso, L., Malá‐Ládová, K., Malý, J., et al. (2022) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2022.2070595 · Cited by 235 · see citing works

Shigella’ s ways of manipulating the host intestinal innate and adaptive immune system: a tool box for survival?

Phalipon, A., & Sansonetti, P. J. (2007) · Immunology and Cell Biology · doi:10.1038/sj.icb7100025 · Cited by 233 · see citing works

Antimicrobial Peptides, Innate Immunity, and the Normally Sterile Urinary Tract

ZASLOFF, M. A. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2007050611 · Cited by 230 · see citing works

Peptides and Peptidomimetics for Antimicrobial Drug Design

Mojsoska, B., & Jenssen, H. (2015) · Pharmaceuticals · doi:10.3390/ph8030366 · Cited by 228 · see citing works

Psoriatic scales: a promising source for the isolation of human skin-derived antimicrobial proteins

Harder, J., & Schröder, J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0704409 · Cited by 227 · see citing works

Fish gelatin: The novel potential applications

Lv, L., Huang, Q.-Y., Ding, W. J., Xiao, X., Zhang, H., & Xiong, L.-X. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103581 · Cited by 227 · see citing works

Synthetic Cationic Peptide IDR-1002 Provides Protection against Bacterial Infections through Chemokine Induction and Enhanced Leukocyte Recruitment

Nijnik, A., Madera, L., Ma, S., Waldbrook, M., Elliott, M. R., Easton, D. M., Mayer, M. L., Mullaly, S. C., Kindrachuk, J., Jenssen, H., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901813 · Cited by 218 · see citing works

Waging War against UropathogenicEscherichia coli: Winning Back the Urinary Tract

Sivick, K. E., & Mobley, H. L. T. (2009) · Infection and Immunity · doi:10.1128/iai.01000-09 · Cited by 214 · see citing works

The expanding world of extracellular traps: not only neutrophils but much more

Goldmann, O., & Medina, E. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00420 · Cited by 215 · see citing works

Potential of immunomodulatory host defense peptides as novel anti-infectives

Easton, D. M., Nijnik, A., Mayer, M. L., & Hancock, R. E. W. (2009) · Trends in biotechnology · doi:10.1016/j.tibtech.2009.07.004 · Cited by 215 · see citing works

Criterion for Amino Acid Composition of Defensins and Antimicrobial Peptides Based on Geometry of Membrane Destabilization

Schmidt, N. W., Mishra, A., Lai, G. H., Davis, M., Sanders, L. K., Tran, D., Garcia, A., Tai, K. P., McCray, P. B., Ouellette, A. J., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja200079a · Cited by 214 · see citing works

Cross-species analysis of the mammalian β-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract

Patil, A. A., Cai, Y., Sang, Y., Blecha, F., & Zhang, G. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00104.2005 · Cited by 211 · see citing works

Vitamin D, the placenta and pregnancy

Liu, N. Q., & Hewison, M. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.11.018 · Cited by 211 · see citing works

Intestinal epithelial barrier and mucosal immunity

Müller, C. A., Autenrieth, I. B., & Peschel, A. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5034-2 · Cited by 207 · see citing works

The intestinal epithelial barrier: How to distinguish between the microbial flora and pathogens

Magalhaes, J. G., Tattoli, I., & Girardin, S. E. (2007) · Seminars in Immunology · doi:10.1016/j.smim.2006.12.006 · Cited by 209 · see citing works

Skin Immunity

Matejuk, A. (2017) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-017-0477-3 · Cited by 217 · see citing works

Lung epithelial cells: therapeutically inducible effectors of antimicrobial defense

Leiva‐Juárez, M. M., Kolls, J. K., & Evans, S. E. (2017) · Mucosal Immunology · doi:10.1038/mi.2017.71 · Cited by 204 · see citing works

The Role of Leukocytes from L-PRP/L-PRF in Wound Healing and Immune Defense: New Perspectives

Bielecki, T., Dohan, D., Everts, P. A., & Wiczkowski, A. (2012) · Current Pharmaceutical Biotechnology · doi:10.2174/138920112800624373 · Cited by 204 · see citing works

Transmembrane Pores Formed by Human Antimicrobial Peptide LL-37

Lee, C.-C., Sun, Y., Qian, S., & Huang, H. W. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.02.018 · Cited by 202 · see citing works

Low serum 25-hydroxyvitamin D at critical care initiation is associated with increased mortality*

Braun, A. B., Gibbons, F. K., Litonjua, A. A., Giovannucci, E. L., & Christopher, K. B. (2011) · Critical Care Medicine · doi:10.1097/ccm.0b013e31822d74f3 · Cited by 201 · see citing works

Fighting infections with vitamin D

ZASLOFF, M. A. (2006) · Nature Medicine · doi:10.1038/nm0406-388 · Cited by 198 · see citing works

Antimicrobial peptides and self-DNA in autoimmune skin inflammation

Gilliet, M. F., & Lande, R. (2008) · Current Opinion in Immunology · doi:10.1016/j.coi.2008.06.008 · Cited by 197 · see citing works

Antimicrobial Peptide Synergies for Fighting Infectious Diseases

Mhlongo, J. T., Waddad, A. Y., Alberício, F., & de la Torre, B. G. (2023) · Advanced Science · doi:10.1002/advs.202300472 · Cited by 196 · see citing works

Bovine milk proteome: Quantitative changes in normal milk exosomes, milk fat globule membranes and whey proteomes resulting from Staphylococcus aureus mastitis

Reinhardt, T. A., Sacco, R. E., Nonnecke, B. J., & Lippolis, J. D. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.02.013 · Cited by 191 · see citing works

Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes

Levy, O. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0604320 · Cited by 190 · see citing works

Cathelicidin impact on inflammatory cells

Agier, J., Efenberger-Szmechtyk, M., & Brzezińska‐Błaszczyk, E. (2015) · Central European Journal of Immunology · doi:10.5114/ceji.2015.51359 · Cited by 188 · see citing works

Cathelicidins - a family of multifunctional antimicrobial peptides

Bals, R., & Wilson, J. M. (2003) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-003-2186-9 · Cited by 427 · see citing works

Cathelicidins: Peptides with Antimicrobial, Immunomodulatory, Anti- Inflammatory, Angiogenic, Anticancer and Procancer Activities

Wong, J. H., Ye, X., & Ng, T. B. (2013) · Current Protein and Peptide Science · doi:10.2174/13892037113149990067 · Cited by 60 · see citing works

The Role of Cathelicidins in the Innate Host Defenses of Mammals

Zanetti, M. (2005) · Current Issues in Molecular Biology · doi:10.21775/cimb.007.179 · Cited by 413 · see citing works

Biologic properties and application prospect of cathelicidin

Li, M. (2006) · Immunological Journal

Cathelicidins: a family of endogenous antimicrobial peptides

Lehrer, R. I., & Ganz, T. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200201000-00004 · Cited by 324 · see citing works